Expression of recombinant human pregnancy-associated plasma protein-A and identification of the proform of eosinophil major basic protein as its physiological inhibitor
about
Pregnancy-associated plasma protein-A2 (PAPP-A2), a novel insulin-like growth factor-binding protein-5 proteinaseCrystal structure of the eosinophil major basic protein at 1.8 A. An atypical lectin with a paradigm shift in specificityMutational analysis of the proteolytic domain of pregnancy-associated plasma protein-A (PAPP-A): classification as a metzincinComplex of pregnancy-associated plasma protein-A and the proform of eosinophil major basic protein. Disulfide structure and carbohydrate attachmentExpression of recombinant murine pregnancy-associated plasma protein-A (PAPP-A) and a novel variant (PAPP-Ai) with differential proteolytic activityA genome-wide scan of Ashkenazi Jewish Crohn's disease suggests novel susceptibility lociRare and low-frequency coding variants alter human adult heightDiscovery and characterization of human antibody inhibitors of pregnancy-associated plasma protein-A.Activity of ulilysin, an archaeal PAPP-A-related gelatinase and IGFBP protease.Inhibition of the proteolytic activity of pregnancy-associated plasma protein-A by targeting substrate exosite binding.Indirect targeting of IGF receptor signaling in vivo by substrate-selective inhibition of PAPP-A proteolytic activityLack of functional pregnancy-associated plasma protein-A (PAPPA) compromises mouse ovarian steroidogenesis and female fertility.Transgenic overexpression of pregnancy-associated plasma protein-A in murine arterial smooth muscle accelerates atherosclerotic lesion developmentPattern of secretion of pregnancy-associated plasma protein-A (PAPP-A) during pregnancies complicated by fetal aneuploidy, in vivo and in vitroStanniocalcin-2 inhibits mammalian growth by proteolytic inhibition of the insulin-like growth factor axis.Extracellular proteases as targets for drug developmentThe role of PAPP-A in the IGF system: location, location, location.Stanniocalcin-1 Potently Inhibits the Proteolytic Activity of the Metalloproteinase Pregnancy-associated Plasma Protein-A.First Trimester Maternal Serum Screening Using Biochemical Markers PAPP-A and Free β-hCG for Down Syndrome, Patau Syndrome and Edward SyndromePAPP-A proteolytic activity enhances IGF bioactivity in ascites from women with ovarian carcinomaInsulin-like growth factor (IGF) binding protein-4 is both a positive and negative regulator of IGF activity in vivo.Mutations in pregnancy-associated plasma protein A2 cause short stature due to low IGF-I availability.Severe preeclampsia-related changes in gene expression at the maternal-fetal interface include sialic acid-binding immunoglobulin-like lectin-6 and pappalysin-2.Expression of a protease-resistant insulin-like growth factor-binding protein-4 inhibits tumour growth in a murine model of breast cancer.Placental regulation of peptide hormone and growth factor activity by proMBP.Pregnancy-associated plasma protein-A and the vulnerable plaque.First trimester combined screening - focus on early biochemistry.The proteolytic activity of pregnancy-associated plasma protein-A is potentially regulated by stanniocalcin-1 and -2 during human ovarian follicle development.Pregnancy-associated plasma protein (PAPP)-A expressed in the mammary gland controls epithelial cell proliferation and differentiation.A substrate specificity-determining unit of three Lin12-Notch repeat modules is formed in trans within the pappalysin-1 dimer and requires a sequence stretch C-terminal to the third module.Surface association of pregnancy-associated plasma protein-A accounts for its colocalization with activated macrophages.Proteinase inhibition by proform of eosinophil major basic protein (pro-MBP) is a multistep process of intra- and intermolecular disulfide rearrangements.The Lin12-notch repeats of pregnancy-associated plasma protein-A bind calcium and determine its proteolytic specificity.Cell surface adhesion of pregnancy-associated plasma protein-A is mediated by four clusters of basic residues located in its third and fourth CCP module.Inhibition of proteolysis by the proform of eosinophil major basic protein (proMBP) requires covalent binding to its target proteinase.Cell surface targeting of pregnancy-associated plasma protein A proteolytic activity. Reversible adhesion is mediated by two neighboring short consensus repeats.Substrate specificity of the metalloproteinase pregnancy-associated plasma protein-A (PAPP-A) assessed by mutagenesis and analysis of synthetic peptides: substrate residues distant from the scissile bond are critical for proteolysisStudies on regulation of IGF (insulin-like growth factor)-binding protein (IGFBP) 4 proteolysis by pregnancy-associated plasma protein-A (PAPP-A) in cells treated with phorbol esterTargeted expression of a protease-resistant IGFBP-4 mutant in smooth muscle of transgenic mice results in IGFBP-4 stabilization and smooth muscle hypotrophy.Women with preeclampsia have increased serum levels of pregnancy-associated plasma protein A (PAPP-A), inhibin A, activin A and soluble E-selectin.
P2860
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P2860
Expression of recombinant human pregnancy-associated plasma protein-A and identification of the proform of eosinophil major basic protein as its physiological inhibitor
description
2000 nî lūn-bûn
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2000 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
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2000 թվականի հոտեմբերին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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2000年论文
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name
Expression of recombinant huma ...... as its physiological inhibitor
@ast
Expression of recombinant huma ...... as its physiological inhibitor
@en
Expression of recombinant huma ...... as its physiological inhibitor
@en-gb
Expression of recombinant huma ...... as its physiological inhibitor
@nl
type
label
Expression of recombinant huma ...... as its physiological inhibitor
@ast
Expression of recombinant huma ...... as its physiological inhibitor
@en
Expression of recombinant huma ...... as its physiological inhibitor
@en-gb
Expression of recombinant huma ...... as its physiological inhibitor
@nl
prefLabel
Expression of recombinant huma ...... as its physiological inhibitor
@ast
Expression of recombinant huma ...... as its physiological inhibitor
@en
Expression of recombinant huma ...... as its physiological inhibitor
@en-gb
Expression of recombinant huma ...... as its physiological inhibitor
@nl
P2093
P2860
P356
P1476
Expression of recombinant huma ...... as its physiological inhibitor
@en
P2093
C A Conover
G J Gleich
L S Laursen
L Sottrup-Jensen
M Christiansen
M T Overgaard
P2860
P304
P356
10.1074/JBC.M001384200
P407
P577
2000-10-06T00:00:00Z